采用体积排阻色谱（SEC）联合多角度激光光散射法(MALLS)技术研究了由微生物转谷氨酰胺酶（MTGase）诱导的β-乳球蛋白的体外交联反应。结果表明，在20 mM二硫苏糖醇（DTT）的存在时，用MTGase处理大约11 h，会逐渐形成高分子量的高聚物或寡聚体，同时β-乳球蛋白会由二聚体向单体转变。在DTT不存在时，同样有这种转变。上述结果表明，MTGase处理可作为一种很有潜力的技术，可于调控许多球蛋白的热稳定性。

The in situ cross-linking reaction of β-lactoglobulin (β-LG) induced by microbial transglutaminase (MTGase) was investigated using size-exclusion chromatography (SEC) combined with multi-angle laser light scattering (MALLS). The results indicated that, in the presence of 20 mM dithiothreitol (DTT), the MTGase treatment up to about 11 h gradually resulted in the formation of biopolymers or oligomers with higher molecular weight (MW), and the transformation of dimeric form of β-LG to its monomeric form. This transformation was also observed in the absence of DTT. These data suggested that MTGase treatment could be utilized as a potential technique to modulate the thermal stability of many globular proteins.